Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR
Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR
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DOI：
10.1073/pnas.0603551103
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发表时间：
2006-12-12
影响因子：
11.1
通讯作者：
Ubbink, Marcellus
中科院分区：
文献类型：
--
作者：
Volkov, Alexander N.;Worrall, Jonathan A. R.;Ubbink, Marcellus
酵母细胞色素c过氧化物酶和异1-细胞色素c的生理复合物是生物电子传递的范例。使用顺磁NMR光谱，我们已经确定了溶液中蛋白质复合物的构象，其显示与在晶体结构中观察到的构象非常相似[Pelletier H，Kraut J（1992）Science 258：1748-1755]。我们的研究结果支持这一观点，即这种瞬态电子转移复合物是动态的。溶液结构代表了蛋白质-蛋白质的主要取向，根据我们的估计，该取向占据了复合物寿命的70%以上，其余时间处于动态相遇状态。基于所观察到的顺磁效应，我们描绘了在相互作用的动态部分期间由蛋白质分子采样的构象空间，为经典布朗动力学研究的理论预测提供了实验支持[Northrup SH，Boles JO，Reynolds JCL（1988）Science 241：67-70]。我们的研究结果证实了这种复合物的动态行为，并提供了一个深入了解的蛋白质复合物在溶液中形成的机制。
The physiological complex of yeast cytochrome c peroxidase and iso-1-cytochrome c is a paradigm for biological electron transfer. Using paramagnetic NMR spectroscopy, we have determined the conformation of the protein complex in solution, which is shown to be very similar to that observed in the crystal structure [Pelletier H, Kraut J (1992) Science 258:1748-1755]. Our results support the view that this transient electron transfer complex is dynamic. The solution structure represents the dominant protein-protein orientation, which, according to our estimates, is occupied for > 70% of the lifetime of the complex, with the rest of the time spent in the dynamic encounter state. Based on the observed paramagnetic effects, we have delineated the conformational space sampled by the protein molecules during the dynamic part of the interaction, providing experimental support for the theoretical predictions of the classical Brownian dynamics study [Northrup SH, Boles JO, Reynolds JCL (1988) Science 241:67-70]. Our findings corroborate the dynamic behavior of this complex and offer an insight into the mechanism of the protein complex formation in solution.